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Literature summary for 1.3.98.3 extracted from

  • Layer, G.; Moser, J.; Heinz, D.W.; Jahn, D.; Schubert, W.D.
    Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of Radical SAM enzymes (2003), EMBO J., 22, 6214-6224.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
pharmacology the structure of HemN sets the stage for the development of inhibitors with antibacterial function due to the uniquely bacterial occurence of the enzyme Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure, co-crystallized with S-adenosyl-L-methionine, hanging-drop vapor diffusion method, X-ray analysis Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
coproporphyrinogen-III + S-adenosyl-L-methionine Escherichia coli HemN catalyzes the essential conversion of coproporphyrinogen-III to protoporphyrinogen IX during heme biosynthesis protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
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?

Organism

Organism UniProt Comment Textmining
Escherichia coli P32131
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-

Purification (Commentary)

Purification (Comment) Organism
recombinant HemN Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
coproporphyrinogen III + 2 S-adenosyl-L-methionine = protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine mechanism Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
coproporphyrinogen-III + S-adenosyl-L-methionine HemN catalyzes the essential conversion of coproporphyrinogen-III to protoporphyrinogen IX during heme biosynthesis Escherichia coli protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
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?
coproporphyrinogen-III + S-adenosyl-L-methionine mechanism, the S-adenosyl-L-methionine sulfonium sulfur is near both the Fe and neighboring sulfur of the cluster allowing single electron transfer from the 4Fe-4S cluster to the S-adenosyl-L-methionine sulfonium. S-adenosyl-L-methionine is cleaved yielding a highly oxidizing 5’-deoxyadenosyl radical, HemN binds a second S-adenosyl-L-methionine immediately adjacent to the first and may thus successively catalyze two propionate decarboxylations. Cofactor geometry required for Radical SAM catalysis, detailed enzyme structure, two distinct domains, domain structure, S-adenosyl-L-methionine binding mode Escherichia coli protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
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?

Subunits

Subunits Comment Organism
monomer monomeric enzyme consisting of two distinct domains Escherichia coli

Synonyms

Synonyms Comment Organism
More belongs to the Radical SAM protein family Escherichia coli

Cofactor

Cofactor Comment Organism Structure
4Fe-4S-center HemN binds a 4Fe-4S cluster through three cysteine residues: Cys-62, Cys-66 and Cys-69, a juxtaposed S-adenosyl-L-methionine coordinates the fourth Fe ion through its amide nitrogen and carboxylate oxygen, detailed binding mode, cofactor geometry required for Radical SAM catalysis Escherichia coli
S-adenosyl-L-methionine HemN contains two S-adenosyl-L-methionine molecules as cofactors, detailed binding mode Escherichia coli